ABHD5 antibody for research

The ABHD5 antibody for research of free fatty acids from stored triglyceride is essential to most cell functions, including growth, metabolism and signaling. This process is triggered by a functional interaction between alpha-beta hydrolase domain-containing 5 (ABHD5) and adipose triglyceride lipase (ATGL) that integrates extracellular signals to regulate the lipid homeostasis of fat and muscle cells9.

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ABHD5 null mutations impair ATGL activation, leading to ectopic lipid accumulation in Arabidopsis1, C. elegans2, mice3, and humans (Chanarin-Dorfman syndrome6). However, the precise molecular basis of ABHD5-ATGL interaction remains unknown. Here, we identified a functional surface on ABHD5 required for ATGL activation independently of its lipid droplet translocation and PLIN protein interaction or allosteric regulation by synthetic ligands.

In Cos7 cells, a chimera containing the 75-C-terminal amino acids of ABHD5 that are conserved in all vertebrates and predicted to be required for lipolysis activation (chimera C) activated ATGL, while full length ABHD5 or a control chimera containing R299N, G328S, or D334G did not. Mutation of ABHD5 residue D334 to alanine, asparagine, or a charged variant (D334E) preserved lipolysis, indicating that ABHD5 requires a negatively charged surface for ATGL activation.

Structural models predicted that a salt-bridge between R299 and G328, adjacent to the charge-preserving D334 site, stabilizes the ligand binding pocket and allows for interaction with ATGL’s phospholipase B active center serine S159. This is consistent with the observation that arginine promotes ATGL activation in a cellular membrane-like system, where it has a high pKa and five potential H-bond donors, whereas lysine only weakly supports this activity.

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